Peptide Peptidase(펩타이드 펩타이드)란 무엇입니까?
Peptide Peptidase 펩타이드 펩타이드 - Sitagliptin (STG) is an inhibitor of dipeptide peptidase (DPP) 4 enzyme used in the treatment of type 2 diabetes. [1]시타글립틴(STG)은 제2형 당뇨병 치료에 사용되는 디펩티드 펩티다제(DPP) 4 효소의 억제제입니다. [1]
protease family signal
However, one member of this protease family, signal peptide peptidase-like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. [1] However, one member of this protease family, signal peptide peptidase-like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. [2] However, one member of this protease family, signal peptide peptidase‐like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. [3]그러나 이 프로테아제 계열의 한 구성원인 신호 펩티드 펩티다제 유사 2c(SPPL2c)는 고아로 남아 있으며 단백질 분해 능력과 생리학적 기능은 여전히 수수께끼입니다. [1] 그러나 이 프로테아제 계열의 한 구성원인 신호 펩티드 펩티다제 유사 2c(SPPL2c)는 고아로 남아 있으며 단백질 분해 능력과 생리학적 기능은 여전히 수수께끼입니다. [2] 그러나 이 프로테아제 계열의 한 구성원인 SPPL2c(signal peptide peptidase-like 2c)는 고아로 남아 있으며 단백질 분해 능력과 생리적 기능은 여전히 수수께끼입니다. [3]
Signal Peptide Peptidase 신호 펩티드 펩티다제
We demonstrate here that HCV core protein interferes with the maturation of major histocompatibility complex (MHC) class I catalyzed by signal peptide peptidase (SPP) and induces degradation via HMG-CoA reductase degradation 1 homolog. [1] A previous study identified that cell surface CD59 staining required the intramembrane protease signal peptide peptidase-like 3 (SPPL3). [2] The nuclear translocation occurs after proteolytic cleavage by proteases including signal peptide peptidase and some cysteine proteases. [3] Moreover, repression of HO-1 nuclear translocation by silencing of signal peptide peptidase (SPP), which is responsible for enzymatic cleavage of the TMS of HO-1, exacerbated endothelial senescence. [4] Signal peptide peptidase-like 2 (SPPL) proteases constitute a subfamily of SPP/SPPL intramembrane proteases which are homologues of the presenilins, the catalytic core of the γ-secretase complex. [5] Concurrently, differential expression of putative salinity responsive genes in common fig were determined; signal peptide peptidase-like 2B ( FcSPPL2B ), dehydration responsive element binding protein ( FcDREB ), calcineurin B-like protein (CBL)-CBL-interacting serine/threonine-protein kinase 11 ( FcCIPK11 ), sorbitol dehydrogenase ( FcSORD ) and dehydrin ( FcDHN ). [6] We previously reported that gK binds to signal peptide peptidase (SPP) and that depletion of SPP reduces HSV-1 infectivity in vivo. [7] Our work shows that, at high cholesterol levels, signal peptide peptidase (SPP) cleaves squalene synthase (SQS), an enzyme that defines the branching point for allocation of isoprenoids to the sterol and non-sterol arms of the mevalonate pathway. [8] One such family is the signal peptide peptidase (SPP) and signal peptide peptidase‐like (SPPL) family. [9] Mutagenesis of this transmembrane (TM) region reveals residues that facilitate XBP1u turnover by an ER-associated degradation route that is dependent on signal peptide peptidase (SPP). [10] Absence of Signal Peptide Peptidase, an Essential Herpes Simplex Virus 1 Glycoprotein K Binding Partner, Reduces Virus Infectivity In Vivo Binding of glycoprotein K (gK) to signal peptide peptidase (SPP), an endoplasmic reticulum protein and a member of the -secretase complex, is required for herpes simplex virus 1 (HSV-1) infectivity in vitro. [11] In this context, we previously identified a non-mutant tumor neoepitope, ppCT16−25, derived from the preprocalcitonin (ppCT) leader sequence and processed independently of proteasomes/TAP by a mechanism involving signal peptidase (SP) and signal peptide peptidase (SPP). [12] ABSTRACT We previously reported that herpes simplex virus (HSV) glycoprotein K (gK) binds to signal peptide peptidase (SPP), also known as minor histocompatibility antigen H13. [13] Ectodomain shedding by the metalloprotease ADAM10 and lysosomal degradation generate membrane-bound N-terminal fragments (NTFs), which we identified as novel substrates of the intramembrane proteases signal peptide peptidase–like 2a and b (SPPL2a/b). [14] However, one member of this protease family, signal peptide peptidase-like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. [15] Importantly, we identify by deletion screening of UPR core genes the signal peptide peptidase Spp1 as a novel key factor that is required for establishing a compatible biotrophic interaction between U. [16] Our previous phage display cDNA screens established the essentiality of Plasmodium falciparum signal peptide peptidase (SPP) in asexual development at the blood stage of malaria infection. [17] SPPL2a (Signal Peptide Peptidase Like 2a) is an intramembrane aspartyl protease engaged in the function of B-cells and dendritic cells. [18] Highlights include the discoveries of (1) a new genetic etiology, autosomal recessive signal peptide peptidase‐like 2 A deficiency, (2) TYK2‐deficient patients with a clinical phenotype of MSMD, (3) an allelic form of partial recessive IFN‐γR2 deficiency, and (4) two forms of syndromic MSMD: RORγ/RORγT and JAK1 deficiencies. [19] However, one member of this protease family, signal peptide peptidase-like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. [20] The aspartyl protease signal peptide peptidase (SPP) has recently been shown to be required for processing of the glycoprotein precursor, Gn/Gc, of Bunyamwera virus and for viral infectivity. [21] Plasmodium falciparum Signal Peptide Peptidase (PfSPP) is an important enzyme to infect red blood. [22] Last 8 residues at C-terminus of immature C protein play a major role in proteasomal degradation of CSFV C protein and determine the cleavage efficiency of C protein by signal peptide peptidase (SPP). [23] However, one member of this protease family, signal peptide peptidase‐like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. [24]우리는 여기에서 HCV 핵심 단백질이 신호 펩티드 펩티다제(SPP)에 의해 촉매되는 주요 조직적합성 복합체(MHC) 클래스 I의 성숙을 방해하고 HMG-CoA 환원효소 분해 1 동족체를 통해 분해를 유도한다는 것을 보여줍니다. [1] 이전 연구에서는 세포 표면 CD59 염색이 막내 프로테아제 신호 펩티드 펩티다제 유사 3(SPPL3)을 필요로 한다는 것을 확인했습니다. [2] nan [3] nan [4] nan [5] nan [6] nan [7] nan [8] 그러한 패밀리 중 하나는 신호 펩티드 펩티다제(SPP) 및 신호 펩티드 펩티다제 유사(SPPL) 패밀리입니다. [9] 이 막횡단(TM) 영역의 돌연변이유발은 신호 펩티드 펩티다제(SPP)에 의존하는 ER 관련 분해 경로에 의해 XBP1u 전환을 촉진하는 잔기를 드러냅니다. [10] nan [11] nan [12] nan [13] nan [14] 그러나 이 프로테아제 계열의 한 구성원인 신호 펩티드 펩티다제 유사 2c(SPPL2c)는 고아로 남아 있으며 단백질 분해 능력과 생리학적 기능은 여전히 수수께끼입니다. [15] nan [16] nan [17] nan [18] nan [19] 그러나 이 프로테아제 계열의 한 구성원인 신호 펩티드 펩티다제 유사 2c(SPPL2c)는 고아로 남아 있으며 단백질 분해 능력과 생리학적 기능은 여전히 수수께끼입니다. [20] nan [21] nan [22] nan [23] 그러나 이 프로테아제 계열의 한 구성원인 SPPL2c(signal peptide peptidase-like 2c)는 고아로 남아 있으며 단백질 분해 능력과 생리적 기능은 여전히 수수께끼입니다. [24]